Anti-GRP75

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Heat shock 70kDa protein 9, also known as GRP75, mot-2, mthsp75, PBP74, HSPA9B, and Mortalin, is a highly conserved member of the HSP70 family of proteins. It functions as a chaperone in the mitochondria, cytoplasm, and centrosome. The HSPA9 gene is mapped to chromosome 5q31.2 based on an alignment of the HSPA9 sequence with the genomic sequence. Knockdown of the protein in erythroid cultures was associated with an increased number of cells in the G0/G1 phase of the cell cycle and accelerated apoptosis. Knockdown of the protein in mouse bone marrow cells followed by transplantation into wildtype recipients also resulted in loss of erythroid cell number. Haploinsufficiency for GRP75 may contribute to abnormal hematopoiesis in myelodysplastic syndromes with deletions spanning chromosome 5q31.2. This protein plays a role in the control of cell proliferation. It may also act as a chaperone. Protein function: Chaperone protein which plays an important role in mitochondrial iron-sulfur cluster (ISC) biogenesis. Interacts with and stabilizes ISC cluster assembly proteins FXN, NFU1, NFS1 and ISCU (PubMed:26702583). Regulates erythropoiesis via stabilization of ISC assembly (PubMed:21123823, PubMed:26702583). May play a role in the control of cell proliferation and cellular aging. [The UniProt Consortium]